› 1ger

X-ray diffraction
1.86Å resolution

THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES

Released:
DOI: 10.2210/pdb1ger/pdb
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PDB entry 1ger coloured by chain, front view.
PDB entry 1ger coloured by chain, side view.
PDB entry 1ger coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes.
Mittl PR, Schulz GE
Protein Sci 3 799-809 (1994)
PMID: 8061609

Function and Biology Details

Reaction catalysed: 
2 glutathione + NADP(+) = glutathione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139154 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 450 amino acids
Theoretical weight: 48.83 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P06715 (Residues: 1-450; Coverage: 100%)
Gene names: JW3467, b3500, gor
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Unit cell:
a: 120.5Å b: 73.6Å c: 60.5Å
α: 90° β: 90° γ: 83°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Not provided

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Citations

8 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
7 more

8 mentions without citation

Simple mechanisms for the evolution of protein complexity.
Pillai et al. (2022)
7 more

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